NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.01845-07; PubMed=18065534 [NCBI, ExPASy, EBI, Israel, Japan]
Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., Nash J.H.E.;
"The complete genome sequence of Actinobacillus pleuropneumoniae L20 (serotype 5b).";
J. Bacteriol. 190:1495-1496(2008).

Comments

FUNCTION: This enzyme catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate (By similarity).
CATALYTIC ACTIVITY: H₂S + 3 NADP⁺ + 3 H₂O = sulfite + 3 NADPH.
COFACTOR: Binds 1 siroheme per subunit (By similarity).
COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
SUBUNIT: Alpha(8)-beta(4). The alpha component is a flavoprotein, the beta component is a hemoprotein (By similarity).
SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000569; ABN74924.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001054529.1; -.

3D structure databases

ModBase

A3N3D8.

Ontologies

GO:0009337;	Cellular component: sulfite reductase complex (NADPH) (inferred from electronic annotation from InterPro).
GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0004783;	Molecular function: sulfite reductase (NADPH) activity (inferred from electronic annotation from HAMAP).
GO:0019344;	Biological process: cysteine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0000103;	Biological process: sulfate assimilation (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01540; -; 1.
PBIL [Tree]

InterPro

IPR011786; CysI.
IPR006066; Nir_Si_BS.
IPR006067; Nir_Sir_4Fe4S.
IPR005117; NiRdtase/SiRdtase_haem-b_fer.
Graphical view of domain structure.

Pfam

PF01077; NIR_SIR; 1.
PF03460; NIR_SIR_ferr; 2.
Pfam graphical view of domain structure.

PR00397; SIROHAEM.

TIGR02041; CysI; 1.

PS00365; NIR_SIR; 1.

Genome annotation databases

GeneID

4848697; -.

GenomeReviews

CP000569_GR; APL_1842.

KEGG

apl:APL_1842; -.

CMR

A3N3D8; APL_1842.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

4Fe-4S; Amino-acid biosynthesis; Complete proteome; Cysteine biosynthesis; Heme; Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 588`	`588`	`Sulfite reductase [NADPH] hemoprotein beta-component.`	`PRO_1000068756`
`METAL`	`442 442`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`448 448`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`487 487`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`491 491`		`Iron (siroheme axial ligand) (By similarity).`
`METAL`	`491 491`		`Iron-sulfur (4Fe-4S) (By similarity).`

Sequence information

Length: 588 AA [This is the length of the unprocessed precursor]

Molecular weight: 66761 Da [This is the MW of the unprocessed precursor]

CRC64: 3CBA5BBE72775200 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSDKKIKGLE WQEKPLSDNE RLKTDSNFLR GTILDDLKDD LTGGFKGDNF QLIRFHGMYE 

        70         80         90        100        110        120 
QDDRDIRAER LEEKLEPLKF MLLRCRLPGG IIKPYQWIEI DKFAREHTRY QSIRLTNRQT 

       130        140        150        160        170        180 
FQYHGVPKGK LQPMHRLLHS IGLDSIATAA DMNRNVLCTS NPIESELHQQ AYEFAKKISE 

       190        200        210        220        230        240 
HLLPRSRGYL DVWVDGKKVE SSDDLLKIED EPILGKTYLP RKFKTAVAIP PLNDVDVYAN 

       250        260        270        280        290        300 
DLNFIAIQDE NGQLCGFNVL VGGGLSFEHG NTKTYPNVAY SLGFVPLEHT LAAAEGVVKT 

       310        320        330        340        350        360 
QRDFGNRSDR KNARVRYTVQ NMTLDGFRAE VERCMNIKFE PTRPYEFTER GDRIGWVKGI 

       370        380        390        400        410        420 
DNNWHLTLFI ESVRITDKPE KPLMTGVLEL AKVHKGDFRI TANQNLIVAN VAEQDKAQIE 

       430        440        450        460        470        480 
AIARQYGLIQ EISKLRENAM SCVSLPTCPL AMAEAERVLP DFISELDKVL SKHNVADESI 

       490        500        510        520        530        540 
ITRITGCPNG CGRAMLAEIG LVGKAIGRYN LHIGGDRAGL RISRLYKENI TLQEIVNEID 

       550        560        570        580 
QLVARWATER QTNEAFGDFV IRSNIIAPVV NAHIDFWDAT KIIPTTII

A3N3D8 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools